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Proteolytic activity in Pacific shrimp (Pandalus jordani) processing waste; distribution, effects on muscle proteins, and partial characterizationDecker, Carl David 27 June 1974 (has links)
Proteases present in shrimp processing waste are factors in the
technology of shrimp. The distribution of proteolytic activity in
shrimp parts was determined using hemoglobin and casein as substrates. The effects of various parameters upon activity of proteases
in the inedible portion were determined using muscle protein as a
substrate. Low pH active proteases from the hepatopancreas were
characterized using column chromatography and inhibitors.
A crude homogenate of shrimp processing waste showed maximum
proteolytic activity on casein at pH 6.25, although activity was
relatively uniform between pH 5.75 and 7.5. Hemoglobin digestion
was greatest between pH 3 and 3.65.
Specific activity was greatest in the foregut followed by the
hepatopancreas and remainder of the inedible portion. Shrimp which
contained food in their foreguts had greatest total activity in the foregut
followed by the hepatopancreas. The order was reversed for
shrimp which had not been feeding. Total activity was lowest in the
inedible portion with digestive organs removed. Only negligible
activity was detected in the muscle.
Autolytic changes in a model system were studied where shrimp
processing waste was the major protease source and muscle protein
served as the major substrate. Activity data showed a major maximum
at pH 3 and a minor broad maximum between pH 7 and 9. Maximum
autolytic activity occurred at 50°C for pH 3 and at 55°C for pH
7.4. Incubation of the inedible portion at 65°C for 30 min was sufficient
to inactivate the proteases. Proteases were unstable at low pH
and 10 min on ice at pH 1.8 were required for inactivation. Autolysis
at pH 3 was completely prevented by 10% NaCl while the inhibitory
effects were less at pH 7.4. Protein solubility was decreased by
NaCl at pH 3 and increased at pH 7.4. Heat-denatured muscle proteins
were less susceptible to hydrolysis, possibly through a reduction in
solubility. Changes occurred in the electrophoretic profile of soluble
proteins (pH 7.4) from a muscle mixture which was incubated at 50°C. Changes also occurred when incubation mixtures contained inedible
portion and these changes were more rapid than when inedible portion was absent.
Low pH active proteases from the hepatopancreas were studied
using hemoglobin as a substrate at pH 3.5. Gel filtration of a preparation
from the hepatopancreas on Sephadex G-150 separated hemoglobin
digesting activity in two distinct fractions. Chromatography
on DEAE-cellulose also separated activity into two fractions and
provided further evidence for the existence of at least two enzymes.
Fractions from chromatography were unaffected by phenylmethyl
sulphonylfluoride, unaffected or slightly activated by KCN, and
greatly inactivated by p-chloromercuribenzoate. EDTA greatly
activated all fractions. The result indicated that -SH groups are
important for enzyme activity. A crude homogenate of the hepatopancreas
and the major fraction from ion-exchange chromatography
were most active on hemoglobin between pH 3 and 4. / Graduation date: 1975
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Engineering highly active and specific protease variantsVaradarajan, Navin, January 1900 (has links) (PDF)
Thesis (Ph. D.)--University of Texas at Austin, 2006. / Vita. Includes bibliographical references.
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Engineering highly active and specific protease variantsVaradarajan, Navin 28 August 2008 (has links)
Not available
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I Inhibition of acid proteases by peptide diazomethyl ketones ; II Investigation of serine protease activity with acyl carbazatesGupton, Bernard Franklin 05 1900 (has links)
No description available.
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Thioesters of amino acids, peptides and p̲a̲r̲a̲-quanidinobenzoic acid as probes of the active sites of serine proteases and metalloproteasesCook, Robert Richard 08 1900 (has links)
No description available.
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The purification and characterization studies on the neutral protease from Bacillus subtilisMcConn, James Dwight January 1965 (has links)
Typescript. / Thesis (Ph. D.)--University of Hawaii, 1965. / Bibliography: leaves 94-97. / [3], xi, 97 l mounted illus., tables
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The purification and substrate specificity of plant proteolytic enzymes / by William Francis Carey.Carey, William Francis January 1971 (has links)
ix, 161 leaves : ill. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.)--University of Adelaide, Dept. of Biochemistry, 1972
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The purification and substrate specificity of plant proteolytic enzymes /Carey, William Francis. January 1971 (has links) (PDF)
Thesis (Ph.D.) -- University of Adelaide, Dept. of Biochemistry, 1972.
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Molecular biology studies on the extracellular serine proteases of Vibrio alginolyticusDeane, Shelly May January 1989 (has links)
Bibliography: pages 161-176. / Vibrio alginolyticus is a gram-negative aerobic bacterium that produces several extracellular serine proteases and a collagenase during the stationary growth phase. The aim of this study was to investigate alkaline serine protease production by this organism, and to attempt the cloning and expression of a V.alginolyticus protease gene in Escherichia coli.
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Identification and characterization of proteolytic enzymes in Trichinella spp賴玉耀, Lai, Yuk-yeu, William. January 1996 (has links)
published_or_final_version / Zoology / Master / Master of Philosophy
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